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Volumn 448, Issue 7152, 2007, Pages 435-438

A lipid-based model for the creation of an escape hatch from the endoplasmic reticulum

Author keywords

[No Author keywords available]

Indexed keywords

FAT DROPLET; LIPID;

EID: 34547216748     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature06004     Document Type: Article
Times cited : (237)

References (45)
  • 3
    • 24944446266 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated degradation
    • Romisch, K. Endoplasmic reticulum-associated degradation. Annu. Rev. Cell Dev. Biol. 21, 435-456 (2005).
    • (2005) Annu. Rev. Cell Dev. Biol , vol.21 , pp. 435-456
    • Romisch, K.1
  • 4
    • 0036270698 scopus 로고    scopus 로고
    • Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
    • Tsai, B., Ye, Y. & Rapoport, T. A. Retro-translocation of proteins from the endoplasmic reticulum into the cytosol. Nature Rev. Mol. Cell Biol. 3, 246-255 (2002).
    • (2002) Nature Rev. Mol. Cell Biol , vol.3 , pp. 246-255
    • Tsai, B.1    Ye, Y.2    Rapoport, T.A.3
  • 5
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard, L. & Helenius, A. Quality control in the endoplasmic reticulum. Nature Rev. Mol. Cell Biol. 4, 181-191 (2003).
    • (2003) Nature Rev. Mol. Cell Biol , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 6
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg, A. L. Protein degradation and protection against misfolded or damaged proteins. Nature 426, 895-899 (2003).
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 7
    • 20444404618 scopus 로고    scopus 로고
    • Regulated protein degradation
    • Varshavsky, A. Regulated protein degradation. Trends Biochem. Sci. 30, 283-286 (2005).
    • (2005) Trends Biochem. Sci , vol.30 , pp. 283-286
    • Varshavsky, A.1
  • 8
    • 3042725669 scopus 로고    scopus 로고
    • Cell biology: A channel for protein waste
    • Schekman, R. Cell biology: a channel for protein waste. Nature 429, 817-818 (2004).
    • (2004) Nature , vol.429 , pp. 817-818
    • Schekman, R.1
  • 9
    • 0029828991 scopus 로고    scopus 로고
    • Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
    • Wiertz, E. J. et al. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 384, 432-438 (1996).
    • (1996) Nature , vol.384 , pp. 432-438
    • Wiertz, E.J.1
  • 10
    • 3042677637 scopus 로고    scopus 로고
    • Amembrane protein complex mediates retro-translocation from the ER lumen into the cytosol
    • Ye, Y., Shibata, Y., Yun, C., Ron, D. & Rapoport, T. A. Amembrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Nature 429, 841-847 (2004).
    • (2004) Nature , vol.429 , pp. 841-847
    • Ye, Y.1    Shibata, Y.2    Yun, C.3    Ron, D.4    Rapoport, T.A.5
  • 11
    • 3042616595 scopus 로고    scopus 로고
    • A membrane protein required for dislocation of misfolded proteins from the ER
    • Lilley, B. N. & Ploegh, H. L. A membrane protein required for dislocation of misfolded proteins from the ER. Nature 429, 834-840 (2004).
    • (2004) Nature , vol.429 , pp. 834-840
    • Lilley, B.N.1    Ploegh, H.L.2
  • 12
    • 0037134014 scopus 로고    scopus 로고
    • Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae
    • Pelkmans, L., Puntener, D. & Helenius, A. Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae. Science 296, 535-539 (2002).
    • (2002) Science , vol.296 , pp. 535-539
    • Pelkmans, L.1    Puntener, D.2    Helenius, A.3
  • 13
    • 33748658449 scopus 로고    scopus 로고
    • Murine polyomavirus requires the endoplasmic reticulum protein Derlin-2 to initiate infection
    • Lilley, B. N., Gilbert, J. M., Ploegh, H. L. & Benjamin, T. L. Murine polyomavirus requires the endoplasmic reticulum protein Derlin-2 to initiate infection. J. Virol. 80, 8739-8744 (2006).
    • (2006) J. Virol , vol.80 , pp. 8739-8744
    • Lilley, B.N.1    Gilbert, J.M.2    Ploegh, H.L.3    Benjamin, T.L.4
  • 14
    • 33750310094 scopus 로고    scopus 로고
    • Downregulation of protein disulfide isomerase inhibits infection by the mouse polyomavirus
    • Gilbert, J., Ou, W., Silver, J. & Benjamin, T. Downregulation of protein disulfide isomerase inhibits infection by the mouse polyomavirus. J. Virol. 80, 10868-10870 (2006).
    • (2006) J. Virol , vol.80 , pp. 10868-10870
    • Gilbert, J.1    Ou, W.2    Silver, J.3    Benjamin, T.4
  • 15
    • 0037113954 scopus 로고    scopus 로고
    • The surface of lipid droplets is a phospholipid monolayer with a unique Fatty Acid composition
    • Tauchi-Sato, K., Ozeki, S., Houjou, T., Taguchi, R. & Fujimoto, T. The surface of lipid droplets is a phospholipid monolayer with a unique Fatty Acid composition. J. Biol. Chem. 277, 44507-44512 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 44507-44512
    • Tauchi-Sato, K.1    Ozeki, S.2    Houjou, T.3    Taguchi, R.4    Fujimoto, T.5
  • 16
    • 33646168160 scopus 로고    scopus 로고
    • Lipid droplets: A unified view of a dynamic organelle
    • Martin, S. & Parton, R. G. Lipid droplets: a unified view of a dynamic organelle. Nature Rev. Mol. Cell Biol. 7, 373-378 (2006).
    • (2006) Nature Rev. Mol. Cell Biol , vol.7 , pp. 373-378
    • Martin, S.1    Parton, R.G.2
  • 18
    • 0035809923 scopus 로고    scopus 로고
    • Accumulation of caveolin in the endoplasmic reticulum redirects the protein to lipid storage droplets
    • Ostermeyer, A. G. et al. Accumulation of caveolin in the endoplasmic reticulum redirects the protein to lipid storage droplets. J. Cell Biol. 152, 1071-1078 (2001).
    • (2001) J. Cell Biol , vol.152 , pp. 1071-1078
    • Ostermeyer, A.G.1
  • 19
    • 2542490433 scopus 로고    scopus 로고
    • Association of stomatin with lipid bodies
    • Umlauf, E. et al. Association of stomatin with lipid bodies. J. Biol. Chem. 279, 23699-23709 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 23699-23709
    • Umlauf, E.1
  • 20
    • 0942287191 scopus 로고    scopus 로고
    • Chinese hamster ovary K2 cell lipid droplets appear to be metabolic organelles involved in membrane traffic
    • Liu, P. et al. Chinese hamster ovary K2 cell lipid droplets appear to be metabolic organelles involved in membrane traffic. J. Biol. Chem. 279, 3787-3792 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 3787-3792
    • Liu, P.1
  • 21
    • 8744267532 scopus 로고    scopus 로고
    • Proteomic analysis of proteins associated with lipid droplets of basal and lipolytically stimulated 3T3-L1 adipocytes
    • Brasaemle, D. L., Dolios, G., Shapiro, L. & Wang, R. Proteomic analysis of proteins associated with lipid droplets of basal and lipolytically stimulated 3T3-L1 adipocytes. J. Biol. Chem. 279, 46835-46842 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 46835-46842
    • Brasaemle, D.L.1    Dolios, G.2    Shapiro, L.3    Wang, R.4
  • 22
    • 0242331729 scopus 로고    scopus 로고
    • Imaging coexisting fluid domains in biomembrane models coupling curvature and line tension
    • Baumgart, T., Hess, S. T. & Webb, W. W. Imaging coexisting fluid domains in biomembrane models coupling curvature and line tension. Nature 425, 821-824 (2003).
    • (2003) Nature , vol.425 , pp. 821-824
    • Baumgart, T.1    Hess, S.T.2    Webb, W.W.3
  • 23
    • 3142516233 scopus 로고    scopus 로고
    • Membrane lipids and vesicular traffic
    • van Meer, G. & Sprong, H. Membrane lipids and vesicular traffic. Curr. Opin. Cell Biol. 16, 373-378 (2004).
    • (2004) Curr. Opin. Cell Biol , vol.16 , pp. 373-378
    • van Meer, G.1    Sprong, H.2
  • 24
    • 0035017308 scopus 로고    scopus 로고
    • Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER
    • Pelkmans, L., Kartenbeck, J. & Helenius, A. Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER. Nature Cell Biol. 3, 473-483 (2001).
    • (2001) Nature Cell Biol , vol.3 , pp. 473-483
    • Pelkmans, L.1    Kartenbeck, J.2    Helenius, A.3
  • 25
    • 0031471055 scopus 로고    scopus 로고
    • Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration
    • Liao, S., Lin, J., Do, H. & Johnson, A. E. Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration. Cell 90, 31-41 (1997).
    • (1997) Cell , vol.90 , pp. 31-41
    • Liao, S.1    Lin, J.2    Do, H.3    Johnson, A.E.4
  • 26
    • 33744928427 scopus 로고    scopus 로고
    • The coxsackievirus 2B protein increases efflux of ions from the endoplasmic reticulum and Golgi, thereby inhibiting protein trafficking through the Golgi
    • de Jong, A. S. et al. The coxsackievirus 2B protein increases efflux of ions from the endoplasmic reticulum and Golgi, thereby inhibiting protein trafficking through the Golgi. J. Biol. Chem. 281, 14144-14150 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 14144-14150
    • de Jong, A.S.1
  • 27
    • 0030928285 scopus 로고    scopus 로고
    • Coxsackievirus protein 2B modifies endoplasmic reticulum membrane and plasma membrane permeability and facilitates virus release
    • van Kuppeveld, F. J. et al. Coxsackievirus protein 2B modifies endoplasmic reticulum membrane and plasma membrane permeability and facilitates virus release. EMBO J. 16, 3519-3532 (1997).
    • (1997) EMBO J , vol.16 , pp. 3519-3532
    • van Kuppeveld, F.J.1
  • 28
    • 0029915568 scopus 로고    scopus 로고
    • The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol
    • Wiertz, E. J. et al. The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol. Cell 84, 769-779 (1996).
    • (1996) Cell , vol.84 , pp. 769-779
    • Wiertz, E.J.1
  • 29
    • 1442313919 scopus 로고    scopus 로고
    • A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised
    • Blom, D., Hirsch, C., Stern, P., Tortorella, D. & Ploegh, H. L. A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised. EMBO J. 23, 650-658 (2004).
    • (2004) EMBO J , vol.23 , pp. 650-658
    • Blom, D.1    Hirsch, C.2    Stern, P.3    Tortorella, D.4    Ploegh, H.L.5
  • 30
    • 10644226176 scopus 로고    scopus 로고
    • Using a small molecule inhibitor of peptide: N-glycanase to probe its role in glycoprotein turnover
    • Misaghi, S., Pacold, M. E., Blom, D., Ploegh, H. L. & Korbel, G. A. Using a small molecule inhibitor of peptide: N-glycanase to probe its role in glycoprotein turnover. Chem. Biol. 11, 1677-1687 (2004).
    • (2004) Chem. Biol , vol.11 , pp. 1677-1687
    • Misaghi, S.1    Pacold, M.E.2    Blom, D.3    Ploegh, H.L.4    Korbel, G.A.5
  • 31
    • 4344657260 scopus 로고    scopus 로고
    • N-linked carbohydrates act as lumenal maturation and quality control protein tags
    • Daniels, R., Svedine, S. & Hebert, D. N. N-linked carbohydrates act as lumenal maturation and quality control protein tags. Cell Biochem. Biophys. 41, 113-138 (2004).
    • (2004) Cell Biochem. Biophys , vol.41 , pp. 113-138
    • Daniels, R.1    Svedine, S.2    Hebert, D.N.3
  • 32
    • 0028921674 scopus 로고
    • The effects of variable glycosylation on the functional activities of ribonuclease, plasminogen and tissue plasminogen activator
    • Rudd, P. M. et al. The effects of variable glycosylation on the functional activities of ribonuclease, plasminogen and tissue plasminogen activator. Biochim. Biophys. Acta 1248, 1-10 (1995).
    • (1995) Biochim. Biophys. Acta , vol.1248 , pp. 1-10
    • Rudd, P.M.1
  • 33
    • 0037470054 scopus 로고    scopus 로고
    • Protein unfolding is not a prerequisite for endoplasmic reticulum-to-cytosol dislocation
    • Tirosh, B., Furman, M. H., Tortorella, D. & Ploegh, H. L. Protein unfolding is not a prerequisite for endoplasmic reticulum-to-cytosol dislocation. J. Biol. Chem. 278, 6664-6672 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 6664-6672
    • Tirosh, B.1    Furman, M.H.2    Tortorella, D.3    Ploegh, H.L.4
  • 34
    • 0036499973 scopus 로고    scopus 로고
    • Visualization of the ER-to-cytosol dislocation reaction of a type I membrane protein
    • Fiebiger, E., Story, C., Ploegh, H. L. & Tortorella, D. Visualization of the ER-to-cytosol dislocation reaction of a type I membrane protein. EMBO J. 21, 1041-1053 (2002).
    • (2002) EMBO J , vol.21 , pp. 1041-1053
    • Fiebiger, E.1    Story, C.2    Ploegh, H.L.3    Tortorella, D.4
  • 35
    • 0041816452 scopus 로고    scopus 로고
    • Ubiquitinylation of the cytosolic domain of a type I membrane protein is not required to initiate its dislocation from the endoplasmic reticulum
    • Furman, M. H., Loureiro, J., Ploegh, H. L. & Tortorella, D. Ubiquitinylation of the cytosolic domain of a type I membrane protein is not required to initiate its dislocation from the endoplasmic reticulum. J. Biol. Chem. 278, 34804-34811 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 34804-34811
    • Furman, M.H.1    Loureiro, J.2    Ploegh, H.L.3    Tortorella, D.4
  • 36
    • 33744755382 scopus 로고    scopus 로고
    • Cytoplasmic lipid droplets are sites of convergence of proteasomal and autophagic degradation of apolipoprotein B
    • Ohsaki, Y., Cheng, J., Fujita, A., Tokumoto, T. & Fujimoto, T. Cytoplasmic lipid droplets are sites of convergence of proteasomal and autophagic degradation of apolipoprotein B. Mol. Biol. Cell 17, 2674-2683 (2006).
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2674-2683
    • Ohsaki, Y.1    Cheng, J.2    Fujita, A.3    Tokumoto, T.4    Fujimoto, T.5
  • 37
    • 33748434907 scopus 로고    scopus 로고
    • Proteasomal and autophagic pathways converge on lipid droplets
    • Fujimoto, T. & Ohsaki, Y. Proteasomal and autophagic pathways converge on lipid droplets. Autophagy 2, 299-301 (2006).
    • (2006) Autophagy , vol.2 , pp. 299-301
    • Fujimoto, T.1    Ohsaki, Y.2
  • 38
    • 33751506565 scopus 로고    scopus 로고
    • Antigen presentation and the ubiquitinproteasome system in host-pathogen interactions
    • Loureiro, J. & Ploegh, H. L. Antigen presentation and the ubiquitinproteasome system in host-pathogen interactions. Adv. Immunol. 92, 225-305 (2006).
    • (2006) Adv. Immunol , vol.92 , pp. 225-305
    • Loureiro, J.1    Ploegh, H.L.2
  • 39
    • 0029001515 scopus 로고
    • Generation, translocation, and presentation of MHC class I-restricted peptides
    • Heemels, M. T. & Ploegh, H. Generation, translocation, and presentation of MHC class I-restricted peptides. Annu. Rev. Biochem. 64, 463-491 (1995).
    • (1995) Annu. Rev. Biochem , vol.64 , pp. 463-491
    • Heemels, M.T.1    Ploegh, H.2
  • 40
    • 0028313992 scopus 로고
    • Assembly, transport, and function of MHC class II molecules
    • Cresswell, P. Assembly, transport, and function of MHC class II molecules. Annu. Rev. Immunol. 12, 259-293 (1994).
    • (1994) Annu. Rev. Immunol , vol.12 , pp. 259-293
    • Cresswell, P.1
  • 41
    • 26244455510 scopus 로고    scopus 로고
    • Mechanisms of MHC class I-restricted antigen processing and cross-presentation
    • Cresswell, P., Ackerman, A. L., Giodini, A., Peaper, D. R. & Wearsch, P. A. Mechanisms of MHC class I-restricted antigen processing and cross-presentation. Immunol. Rev. 207, 145-157 (2005).
    • (2005) Immunol. Rev , vol.207 , pp. 145-157
    • Cresswell, P.1    Ackerman, A.L.2    Giodini, A.3    Peaper, D.R.4    Wearsch, P.A.5
  • 42
    • 3242804567 scopus 로고    scopus 로고
    • Cellular mechanisms governing cross-presentation of exogenous antigens
    • Ackerman, A. L. & Cresswell, P. Cellular mechanisms governing cross-presentation of exogenous antigens. Nature Immunol. 5, 678-684 (2004).
    • (2004) Nature Immunol , vol.5 , pp. 678-684
    • Ackerman, A.L.1    Cresswell, P.2
  • 43
    • 0141707939 scopus 로고    scopus 로고
    • ER-phagosome fusion defines an MHC class I cross-presentation compartment in dendritic cells
    • Guermonprez, P. et al. ER-phagosome fusion defines an MHC class I cross-presentation compartment in dendritic cells. Nature 425, 397-402 (2003).
    • (2003) Nature , vol.425 , pp. 397-402
    • Guermonprez, P.1
  • 44
    • 12444339508 scopus 로고    scopus 로고
    • Exogenous antigens are processed through the endoplasmic reticulum-associated degradation (ERAD) in cross-presentation by dendritic cells
    • Imai, J., Hasegawa, H., Maruya, M., Koyasu, S. &Yahara, I. Exogenous antigens are processed through the endoplasmic reticulum-associated degradation (ERAD) in cross-presentation by dendritic cells. Int. Immunol. 17, 45-53 (2005).
    • (2005) Int. Immunol , vol.17 , pp. 45-53
    • Imai, J.1    Hasegawa, H.2    Maruya, M.3    Koyasu, S.4    Yahara, I.5
  • 45
    • 33749522738 scopus 로고    scopus 로고
    • A role for the endoplasmic reticulum protein retrotranslocation machinery during crosspresentation by dendritic cells
    • Ackerman, A. L., Giodini, A. & Cresswell, P. A role for the endoplasmic reticulum protein retrotranslocation machinery during crosspresentation by dendritic cells. Immunity 25, 607-617 (2006).
    • (2006) Immunity , vol.25 , pp. 607-617
    • Ackerman, A.L.1    Giodini, A.2    Cresswell, P.3


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